Record ID | ia:hemeperoxidases0000dunf |
Source | Internet Archive |
Download MARC XML | https://archive.org/download/hemeperoxidases0000dunf/hemeperoxidases0000dunf_marc.xml |
Download MARC binary | https://www.archive.org/download/hemeperoxidases0000dunf/hemeperoxidases0000dunf_meta.mrc |
LEADER: 03935cam 2200529 a 4500
001 ocm39323127
003 OCoLC
005 20200527220038.0
008 980616s1999 nyua b 001 0 eng
010 $a 98028908
040 $aDLC$beng$cDLC$dUKM$dBAKER$dBTCTA$dYDXCP$dDEBBG$dOCLCF$dCOF$dOCLCQ$dGZM$dOCLCQ$dLGG$dSFB
015 $aGB9930181$2bnb
019 $a822884614
020 $a0471242446$q(cloth ;$qalk. paper)
020 $a9780471242444$q(cloth ;$qalk. paper)
035 $a(OCoLC)39323127$z(OCoLC)822884614
050 00 $aQP603.P4$bD86 1999
060 4 $aQU 140$bD915h 1999
082 00 $a572/.791$221
100 1 $aDunford, H. Brian.
245 10 $aHeme peroxidases /$cH. Brian Dunford.
260 $aNew York :$bJohn Wiley,$c©1999.
300 $axiii, 507 pages :$billustrations ;$c25 cm
336 $atext$btxt$2rdacontent
337 $aunmediated$bn$2rdamedia
338 $avolume$bnc$2rdacarrier
504 $aIncludes bibliographical references and index.
505 0 $a1. Introduction. Historical Background -- 2. Model Peroxidases from Yeast and Horseradish, Cloned Enzymes, and Comparison to Metmyoglobin -- 3. Heme Peroxidase and Catalase Families and Superfamilies: Crystal Structures -- 4. Horseradish Peroxidase. I: Ligand Binding, Redox Potentials, Formation of Its Compounds, and Some of Their Reactions -- 5. Horseradish Peroxidase. II: Isoenzymes, Steady-State Kinetics, and Peroxidase-Oxidase Reaction -- 6. Horseradish Peroxidase. III: Reaction with Indole-3-Acetic Acid, Light Emission, and Quantitative Structure-Activity Relationships -- 7. Spectroscopy of Horseradish Peroxidase. I: Optical, Resonance Raman, Magnetic Circular Dichroism, X-ray Absorption, and Diffraction -- 8. Spectroscopy of Horseradish Peroxidase. II: Nuclear Magnetic Resonance, Electron Paramagnetic Resonance, Electron Nuclear Double Resonance, Mossbauer Spectroscopy, and Theoretical Studies -- 9. Yeast Cytochrome c Peroxidase. I: Properties and Reactions with Small Molecules -- 10. Yeast Cytochrome c Peroxidase. II: Interaction with Cytochrome c -- 11. Other Class I Peroxidases: Ascorbate Peroxidase and Bacterial Catalase-Peroxidases -- 12. Class II Peroxidases: Lignin, Manganese, and Coprinus cinereus Peroxidases -- 13. Other Class III Plant Peroxidases: Peanut, Barley, Tobacco, and Arabidopsis thaliana -- 14. Chloroperoxidase and Pseudomonas Cytochrome c Peroxidase -- 15. Myeloperoxidase and Eosinophil Peroxidase: Phagocytosis and Microbial Killing -- 16. Prostaglandin Endoperoxide H Synthases -- 17. Lactoperoxidase, Thyroid Peroxidase, and Other Animal Peroxidases -- 18. Catalases
650 0 $aPeroxidase.
650 7 $aPeroxidase.$2fast$0(OCoLC)fst01058324
776 08 $iOnline version:$aDunford, H. Brian.$tHeme peroxidases.$dNew York : John Wiley, ©1999$w(OCoLC)742273023
856 41 $3Table of contents$uhttp://catdir.loc.gov/catdir/toc/onix03/98028908.html
856 41 $3Table of contents$uhttp://bvbr.bib-bvb.de:8991/F?func=service&doc_library=BVB01&doc_number=008840038&line_number=0001&func_code=DB_RECORDS&service_type=MEDIA
856 41 $3Table of contents$uhttp://bvbr.bib-bvb.de:8991/F?func=service&doc_library=BVB01&local_base=BVB01&doc_number=008840038&line_number=0001&func_code=DB_RECORDS&service_type=MEDIA
856 42 $3Contributor biographical information$uhttp://catdir.loc.gov/catdir/bios/wiley044/98028908.html
856 42 $3Publisher description$uhttp://catdir.loc.gov/catdir/description/wiley037/98028908.html
938 $aBaker & Taylor$bBKTY$c260.00$d260.00$i0471242446$n0003182123$sactive
938 $aBaker and Taylor$bBTCP$n98028908
938 $aYBP Library Services$bYANK$n100147446
029 1 $aAU@$b000013967360
029 1 $aDEBBG$bBV012975599
029 1 $aHEBIS$b079061214
029 1 $aNZ1$b222234
029 1 $aYDXCP$b100147446
029 1 $aZWZ$b046119574
994 $aZ0$bP4A
948 $hNO HOLDINGS IN P4A - 122 OTHER HOLDINGS